Isothermal titration calorimetry of membrane proteins - Progress and challenges

Krishna Rajarathnam, Jörg Rösgen

Research output: Contribution to journalReview article

50 Scopus citations

Abstract

Integral membrane proteins, including G protein-coupled receptors (GPCR) and ion channels, mediate diverse biological functions that are crucial to all aspects of life. The knowledge of the molecular mechanisms, and in particular, the thermodynamic basis of the binding interactions of the extracellular ligands and intracellular effector proteins is essential to understand the workings of these remarkable nanomachines. In this review, we describe how isothermal titration calorimetry (ITC) can be effectively used to gain valuable insights into the thermodynamic signatures (enthalpy, entropy, affinity, and stoichiometry), which would be most useful for drug discovery studies, considering that more than 30% of the current drugs target membrane proteins. This article is part of a Special Issue entitled: Structural and biophysical characterisation of membrane protein-ligand binding.

Original languageEnglish (US)
Pages (from-to)69-77
Number of pages9
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1838
Issue number1 PARTA
DOIs
StatePublished - Jan 1 2014

Keywords

  • Affinity
  • Drug discovery
  • Enthalpy
  • Isothermal titration calorimetry (ITC)
  • Membrane proteins
  • Thermodynamics

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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